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P31896 (COOS_RHORU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Carbon monoxide dehydrogenase
Short name=CODH
EC=1.2.99.2
Gene names
Name:cooS
OrganismRhodospirillum rubrum
Taxonomic identifier1085 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Rhodospirillum

Protein attributes

Sequence length639 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Allows growth in a CO-dependent manner in the dark. CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).

Catalytic activity

CO + H2O + A = CO2 + AH2.

Cofactor

Binds 3 4Fe-4S clusters per homodimer.

Binds 2 nickel-iron-sulfur clusters per homodimer.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note: Loosely attached to the inner membrane, probably via CooF By similarity.

Induction

By carbon monoxide; under anaerobic conditions.

Domain

Cluster B is an all-cysteinyl-liganded 4Fe4S cluster; cluster C is a mixed Ni-Fe-S cluster which appears to be the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe4S cluster that bridges the two subunits of the CODH dimer.

Miscellaneous

Methyl viologen can act as acceptor. Inactivated by O2.

Sequence similarities

Belongs to the Ni-containing carbon monoxide dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 639639Carbon monoxide dehydrogenase
PRO_0000157139

Sites

Metal binding411Iron-sulfur 1 (4Fe-4S); shared with dimeric partner
Metal binding491Iron-sulfur 1 (4Fe-4S); shared with dimeric partner
Metal binding501Iron-sulfur 2 (4Fe-4S)
Metal binding531Iron-sulfur 2 (4Fe-4S)
Metal binding581Iron-sulfur 2 (4Fe-4S)
Metal binding721Iron-sulfur 2 (4Fe-4S)
Metal binding2651Nickel-iron-sulfur (Ni-4Fe-4S); via tele nitrogen
Metal binding3001Nickel-iron-sulfur (Ni-4Fe-4S)
Metal binding3381Nickel-iron-sulfur (Ni-4Fe-4S)
Metal binding4511Nickel-iron-sulfur (Ni-4Fe-4S)
Metal binding4811Nickel-iron-sulfur (Ni-4Fe-4S)
Metal binding5311Nickel-iron-sulfur (Ni-4Fe-4S)

Experimental info

Mutagenesis2651H → V: Great decrease in activity; diminishes incorporation of nickel. Displays hydroxylamine reductase activity. Ref.3
Mutagenesis5311C → A: Displays hydrogenase activity. Ref.4

Secondary structure

1 ............................................................................................... 639
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31896 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: DCADD7C13D8D85B8

FASTA63966,854
        10         20         30         40         50         60 
MTHHDCAHCS SDACATEMLN LAEANSIETA WHRYEKQQPQ CGFGSAGLCC RICLKGPCRI 

        70         80         90        100        110        120 
DPFGEGPKYG VCGADRDTIV ARHLVRMIAA GTAAHSEHGR HIALAMQHIS QGELHDYSIR 

       130        140        150        160        170        180 
DEAKLYAIAK TLGVATEGRG LLAIVGDLAA ITLGDFQNQD YDKPCAWLAA SLTPRRVKRL 

       190        200        210        220        230        240 
GDLGLLPHNI DASVAQTMSR THVGCDADPT NLILGGLRVA MADLDGSMLA TELSDALFGT 

       250        260        270        280        290        300 
PQPVVSAANL GVMKRGAVNI AVNGHNPMLS DIICDVAADL RDEAIAAGAA EGINIIGICC 

       310        320        330        340        350        360 
TGHEVMMRHG VPLATNYLSQ ELPILTGALE AMVVDVQCIM PSLPRIAECF HTQIITTDKH 

       370        380        390        400        410        420 
NKISGATHVP FDEHKAVETA KTIIRMAIAA FGRRDPNRVA IPAFKQKSIV GFSAEAVVAA 

       430        440        450        460        470        480 
LAKVNADDPL KPLVDNVVNG NIQGIVLFVG CNTTKVQQDS AYVDLAKSLA KRNVLVLATG 

       490        500        510        520        530        540 
CAAGAFAKAG LMTSEATTQY AGEGLKGVLS AIGTAAGLGG PLPLVMHMGS CVDNSRAVAL 

       550        560        570        580        590        600 
ATALANKLGV DLSDLPLVAS APECMSEKAL AIGSWAVTIG LPTHVGSVPP VIGSQIVTKL 

       610        620        630 
VTETAKDLVG GYFIVDTDPK SAGDKLYAAI QERRAGLGL

« Hide

References

[1]"Genetic and physiological characterization of the Rhodospirillum rubrum carbon monoxide dehydrogenase system."
Kerby R.L., Hong S.S., Ensign S.A., Coppoc L.J., Ludden P.W., Roberts G.P.
J. Bacteriol. 174:5284-5294(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: UR1.
[2]"Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme."
Fox J.D., Kerby R.L., Roberts G.P., Ludden P.W.
J. Bacteriol. 178:1515-1524(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: UR1.
[3]"Substitution of valine for histidine 265 in carbon monoxide dehydrogenase from Rhodospirillum rubrum affects activity and spectroscopic states."
Spangler N.J., Meyers M.R., Gierke K.L., Kerby R.L., Roberts G.P., Ludden P.W.
J. Biol. Chem. 273:4059-4064(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-265.
[4]"Converting the NiFeS carbon monoxide dehydrogenase to a hydrogenase and a hydroxylamine reductase."
Heo J., Wolfe M.T., Staples C.R., Ludden P.W.
J. Bacteriol. 184:5894-5897(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-531.
[5]"CO dehydrogenase."
Ferry J.G.
Annu. Rev. Microbiol. 49:305-333(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[6]"Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase."
Drennan C.L., Heo J., Sintchak M.D., Schreiter E., Ludden P.W.
Proc. Natl. Acad. Sci. U.S.A. 98:11973-11978(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U65510 Genomic DNA. Translation: AAC45123.1.
PIRC42957.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JQKX-ray2.80A/B/C/D/E/F1-639[»]
DisProtDP00239.
ProteinModelPortalP31896.
SMRP31896. Positions 28-637.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16431.

Family and domain databases

Gene3D1.20.1270.30. 1 hit.
3.40.50.2030. 2 hits.
InterProIPR016101. CO_DH_a-bundle.
IPR010047. CODH.
IPR004137. HCP/CODH.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
[Graphical view]
PfamPF03063. Prismane. 1 hit.
[Graphical view]
PIRSFPIRSF005023. CODH. 1 hit.
SUPFAMSSF56821. Prismane_like. 1 hit.
TIGRFAMsTIGR01702. CO_DH_cata. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP31896.

Entry information

Entry nameCOOS_RHORU
AccessionPrimary (citable) accession number: P31896
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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